Interactions between milk serum proteins and synthetic fat globule membrane during heating of homogenized whole milk

Abstract

Interaction of serum proteins with the fat globule membranes (FGM) in homogenized whole milk affects the properties of a number of dairy products. The reactions of synthetic FGM in homogenized heated milk were investigated by quantitative analysis of the fat globules using electrophoresis and densitometry. The results indicated that only caseins constituted the newly formed surface of synthetic fat globules after homogenization. The serum proteins (beta-lactoglobulin and alpha-lactalbumin) adsorbed to the FGM only when the fat globules had been heated above 70 degrees C. The alpha s2- and k-caseins and the serum proteins were only slightly dissociated when fat globules were washed in dissociating buffer solutions containing urea and EDTA, confirming that the denatured serum proteins attached to cysteine-containing caseins on FGM. The kinetics of deposition of beta-lactoglobulin and alpha-lactalbumin on the FGM during heating of homogenized milk at 75 degrees C followed a pseudo-first-order reaction, when considered in terms of vacant sites on the fat globule surface. At lower temperatures, kinetics of deposition of the two proteins were similar.